MersV1, France, Analysis, bibRecord, 000366

Hybridization specificity, enzymatic activity and biological (Ha-ras) activity of oligonucleotides containing 2,4-dideoxy-β-D-erythro-hexopyranosyl nucleosides

Identifieur interne : 000366 ( France/Analysis ); précédent : 000365; suivant : 000367

Hybridization specificity, enzymatic activity and biological (Ha-ras) activity of oligonucleotides containing 2,4-dideoxy-β-D-erythro-hexopyranosyl nucleosides

Auteurs : K. Augustyns [France] ; G. Godard [France] ; C. Hendrix [France] ; A. Van Aerschot [France] ; J. Rozenski [France] ; T. Saison-Behmoaras [France] ; P. Herdewijn [France]

Source :

Nucleic Acids Research [ 0305-1048 ] ; 1993.

RBID : ISTEX:7A20AA50114BEDA62F7B1EFDE2DC140F8C6399E9

Abstract

Antisense oligonucleotides with a 2,4-dideoxyhexopyranosyl nucleoside incorporated at the 3'-end and at a mutation site of the Ha-ras oncogene mRNA were synthesized. Melting temperature studies revealed that an A*-G mismatch is more stable than an A*-T mismatch with these hexopyranosyl nucleosides incorporated at the mutation site. The oligonucleotides are stable against enzymatic degradation. RNase H mediated cleavage studies revealed selective cleavage of mutated Ha-ras mRNA. The oligonucleotide containing two pyranose nucleosides at the penultimate position activates RNase H more strongly than natural oligonucleotides. No correlation, however, was found between DNA-DNA or RNA-DNA melting temperatures and RNase H mediated cleavage capacity. Although the A*-G mismatch gives more stable hybridization than the A*-T base pairing, only the oligonucleotides containing an A*-T base pair are recognized by RNase H. This modification is situated 3 base pairs upstream to the cleavage site. Finally, the double pyranose modified oligonucleotide was able to reduce the growth of T24 cells (bladder carcinoma) while the unmodified antisense oligonucleotide was not.

Url:

https://api.istex.fr/ark:/67375/HXZ-PJZP6NV7-B/fulltext.pdf

DOI: 10.1093/nar/21.20.4670

Affiliations:

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to stream Main, to step Merge: 004641
to stream Main, to step Curation: 004575
to stream Main, to step Exploration: 004575
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ISTEX:7A20AA50114BEDA62F7B1EFDE2DC140F8C6399E9

Le document en format XML

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<front><div type="abstract">Antisense oligonucleotides with a 2,4-dideoxyhexopyranosyl nucleoside incorporated at the 3'-end and at a mutation site of the Ha-ras oncogene mRNA were synthesized. Melting temperature studies revealed that an A*-G mismatch is more stable than an A*-T mismatch with these hexopyranosyl nucleosides incorporated at the mutation site. The oligonucleotides are stable against enzymatic degradation. RNase H mediated cleavage studies revealed selective cleavage of mutated Ha-ras mRNA. The oligonucleotide containing two pyranose nucleosides at the penultimate position activates RNase H more strongly than natural oligonucleotides. No correlation, however, was found between DNA-DNA or RNA-DNA melting temperatures and RNase H mediated cleavage capacity. Although the A*-G mismatch gives more stable hybridization than the A*-T base pairing, only the oligonucleotides containing an A*-T base pair are recognized by RNase H. This modification is situated 3 base pairs upstream to the cleavage site. Finally, the double pyranose modified oligonucleotide was able to reduce the growth of T24 cells (bladder carcinoma) while the unmodified antisense oligonucleotide was not.</div>
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Hybridization specificity, enzymatic activity and biological (Ha-ras) activity of oligonucleotides containing 2,4-dideoxy-β-D-erythro-hexopyranosyl nucleosides

Hybridization specificity, enzymatic activity and biological (Ha-ras) activity of oligonucleotides containing 2,4-dideoxy-β-D-erythro-hexopyranosyl nucleosides

Source :

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri